In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria
Abstract
The field of structural biology is increasingly focusing on studying proteins in situ, i.e., in their greater biological context. Cross-linking mass spectrometry (CLMS) is contributing to this effort, typically through the use of mass spectrometry (MS)-cleavable cross-linkers. Here, we apply the popular noncleavable cross-linker disuccinimidyl suberate (DSS) to human mitochondria and identify 5518 distance restraints between protein residues....
Paper Details
Title
In Situ Structural Restraints from Cross-Linking Mass Spectrometry in Human Mitochondria
Published Date
Nov 20, 2019
Journal
Volume
19
Issue
1
Pages
327 - 336
Citation AnalysisPro
You’ll need to upgrade your plan to Pro
Looking to understand the true influence of a researcher’s work across journals & affiliations?
- Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
- Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.
Notes
History